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GenomicsIdentification of 67 histone marks and histone lysine crotonylation as a new type of histone modification
We report the identification of 67 previously undescribed histone modifications, increasing the current number of known histone marks by about 70%. We further investigated one of the marks, lysine crotonylation (Kcr), confirming that it represents an evolutionarily-conserved histone posttranslationa...
ORGANISM(S): Mus musculus 
2011-10-06 | E-GEOD-32663 | biostudies-arrayexpress
UnknownComputational identification of multiple lysine PTM sites by analyzing the instance hardness and feature importance.
Not available
S-EPMC8460736 | biostudies-literature
TranscriptomicsGlobal Identification of Protein PTMs in a Single-pass Database Search
Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify posttranslational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables Global PTM (G-PTM) identification by excl...
ORGANISM(S): Mus musculus 
2015-07-31 | E-GEOD-59956 | biostudies-arrayexpress
UnknownEvolution of a mass spectrometry-grade protease with PTM-directed specificity.
Not available
S-EPMC5187733 | biostudies-literature
ProteomicsSystems level analysis of histone H3 post-translational modifications reveals features of PTM crosstalk in chromatin regulation
Chromatin structure and function is maintained by dynamic protein-protein and protein-nucleic acid interactions. Histones are a family of proteins that are abundant chromatin constituents and that carry numerous post-translational modifications (PTMs). Histone PTMs mediate a variety of biological ac...
ORGANISM(S): Mus musculus (Mouse) 
2016-06-16 | PXD002560 | Pride
Post-translational modification  crosstalk  histone  mass spectrometry  proteomics 
TranscriptomicsGlobal Identification of Protein PTMs in a Single-pass Database Search
Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify posttranslational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables Global PTM (G-PTM) identification by excl...
ORGANISM(S): Mus musculus 
2015-07-31 | GSE59956 | GEO
UnknownRMTLysPTM: recognizing multiple types of lysine PTM sites by deep analysis on sequences.
Not available
S-EPMC10783864 | biostudies-literature
ProteomicsAn Integrated Workflow for Analysis of Multiple Protein Post-Translational Modifications
Investigating multiple protein post-translational modifications (PTMs) is critical for unraveling the complexities of protein regulation and the dynamic interplay among PTMs, a growing focus in proteomics. However, simultaneous analysis of diverse PTMs remains a significant technical challenge, as e...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2026-02-16 | PXD061601 | Pride
Lc-ms/ms Dia Tmt Ptm Pdx Dda 
ProteomicsQuantitative PTM Maps of Human Pathologic Tau Identify Patient Heterogeneity and Define Critical Steps in Alzheimer’s Disease Progression - angular gyrus
To elucidate the role of Tau isoforms and PTM stoichiometry in Alzheimer’s disease (AD), we generated a high resolution quantitative proteomic map of 88 PTMs on multiple isoforms of Tau isolated from the post-mortem human tissue from 49 AD and 42 control subjects. While Tau PTM maps reveal heterogen...
ORGANISM(S): Homo sapiens (Human) 
2020-12-04 | PXD020517 | Pride
Alzheimer's disease  post-translational modification  clinical progression  srm  lfq  human tau  protein aggregation  proteopathy 
ProteomicsA PTM-centric Proteome Informatic Pipeline for Monitoring Post-Translational Modifications by PEIMAN2
Post-translational modifications (PTMs) are under significant focus in molecular biomedicine due to their importance in signal transduction in most cellular and organismal processes. Identification of PTMs, determination of PTM location sites, discrimination between functional and inert PTMs, and qu...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD037681 | Pride
Ptm Proteomics Mass spectromtery 
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